中国农业科学院农业信息研究所 中国农学会
Agricultural Information Institute of CAAS China Association of Agricultural Science Societies
En
Ch
中国农业科学院农业信息研究所 中国农学会 主办

AI检索

订阅

返回顶部
当前位置: 首页 > 文章 > 基于拉曼光谱解析冻藏过程中鱼糜蛋白的结构变化 食品科学 2018 (24) 71-77
Position: Home > Articles > Analysis of Structural Changes of Surimi Proteins during Frozen Storage by Raman Spectroscopy FOOD SCIENCE 2018 (24) 71-77

基于拉曼光谱解析冻藏过程中鱼糜蛋白的结构变化

作  者：
高文宏;叶瑞森;潘廷跳;曾新安
单  位：
华南理工大学食品科学与工程学院
关键词：
拉曼光谱;蛋白结构;冻藏;草鱼鱼糜;氨基酸残基
摘  要：
采用拉曼光谱技术研究冻藏过程中草鱼鱼糜蛋白结构和氨基酸残基微环境的变化。草鱼鱼糜经-18℃冻藏处理2周和8周后进行拉曼光谱扫描,得到光谱数据;对酰胺III区及C—C、S—S、C—H伸缩振动谱带进行解析,对比I_(850)/I_(830)强度变化,同时对酰胺I区蛋白质二级结构进行定量分析。结果表明:冻藏过程中草鱼鱼糜蛋白质主链构象由有序向无序发展,α-螺旋结构从新鲜状态的34.31%下降到冻藏8周后的15.33%,无规卷曲相对含量从13.47%上升到30.89%;新鲜、冻藏2周和冻藏8周的鱼糜蛋白I_(850)/I_(830)分别为1.81、1.89和1.99,鱼糜加工过程使酪氨酸残基暴露在多肽链表面,冻藏引起暴露更加彻底;部分二硫键构象在冻藏初期(2周内)基本完成由反式-扭式-反式向扭式-扭式-反式转变;2 900 cm~(-1)附近C—H伸缩振动的拉曼峰减弱,芳香族氨基酸侧链疏水作用力增强。冻藏过程中鱼糜蛋白的结构逐渐疏散无序,氨基酸残基微环境发生改变。
译  名：
Analysis of Structural Changes of Surimi Proteins during Frozen Storage by Raman Spectroscopy
作  者：
GAO Wenhong;YE Ruisen;PAN Tingtiao;ZENG Xin'an;School of Food Science and Engineering, South China University of Technology;
单  位：
GAO Wenhong%YE Ruisen%PAN Tingtiao%ZENG Xin'an%School of Food Science and Engineering, South China University of Technology
关键词：
Raman spectroscopy;;protein structure;;frozen storage;;grass carp surimi;;amino acid residue
摘  要：
In this paper Raman spectroscopy was used to study the changes of protein structure and amino acid residue microenvironment in grass carp surimi during frozen storage. Grass carp surimi was frozen at-18 ℃ for 2 or 8 weeks and then scanned with a Raman spectrometer. The amide III region, C—C, S—S, and C—H stretching vibration bands were analyzed as well in the variation in I_(850)/I_(830) intensity ratio, and the secondary structures of proteins in the amide I region were quantified. The results showed that the protein backbone conformation was transformed from an ordered to disordered state. The contents of α-helix and random coil structure in fresh surimi were 34.31% and 13.47%, respectively, which decreased to 15.33% and increased to 30.89% after 8 weeks of frozen storage, respectively. The I_(850)/I_(830) intensity ratio was 1.81, 1.89 and 1.99 for fresh, two-week-frozen and eight-week-frozen surimi, respectively. Tyrosine residues were exposed to the surface of polypeptide chains during surimi processing and this phenomenon was more significant after frozen storage. The conformation of some disulfide bonds was transformed from trans-gauche-trans to gauche-gauche-trans within 2 weeks of frozen storage. The Raman peak of C—H stretching vibration near 2 900 cm~(-1) was weakened whereas the hydrophobic interaction of aromatic amino acid side chains was enhanced. The structure of surimi proteins became disorderly and scattered with micro-environmental changes of amino acid residues during frozen storage.

相似文章

导出引用
计量
文章访问数: 13
HTML全文浏览量: 0
PDF下载量: 0

所属期刊

推荐期刊

友情链接Friendly link
农业信息研究所Agricultural information institute 农业智能知识服务平台Agricultural intelligent knowledge service platform 农业学术服务平台Agricultural Knowledge Service System 中国知网CNKI 维普网VIP 万方WANFANG DATA
联系我们Contact us

电话Tell：010-82109652-808

邮箱E-mail：agrijournal@caas.cn

服务Service
关于我们About us 意见建议Opinions and suggest
版权说明Copyright
单位：中国农业科学院农业信息研究所 中国农学会 © 2017中国农业科学院农业信息研究所 ICP备案号：京ICP备09089781号-46